ArticleMolecular biology of the cell2016
Tau antagonizes end-binding protein tracking at microtubule ends through a phosphorylation-dependent mechanism.
Article in Molecular biology of the cell, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
44 citing papers in PubMed, 65 citations in OpenAlex.
- ENKD1 Modulates Skin Elasticity Through Microtubule Stability Regulation.Cytoskeleton (Hoboken, N.J.) · 2026Article
- Dysregulation of the Tau-Microtubule-End-Binding Protein Axis in Alzheimer's Disease and Related Tauopathies.International journal of molecular sciences · 2026Review
- A coherent structural picture of the interaction of Tau with tubulin provides a link to its aggregation.The Journal of biological chemistry · 2026Review
- Altered trafficking of Kv1-Kvβ2 leads to neuronal hyperexcitability and memory deficits in amyloid-β pathology.Molecular neurodegeneration · 2026Article
- L-Dopa-modified microtubules lead to synapse instability in cultured neurons: possible implications in Parkinson's disease therapy.NPJ Parkinson's disease · 2025Article
- TDP-43 dysregulation of polyadenylation site selection is a defining feature of RNA misprocessing in amyotrophic lateral sclerosis and frontotemporal dementia.The Journal of clinical investigation · 2025Article
- Cytoskeleton dysfunction of motor neuron in spinal muscular atrophy.Journal of neurology · 2024Review
- The structure of a Tau fragment bound to tubulin prompts new hypotheses on Tau mechanism and oligomerization.PNAS nexus · 2024Article
- Prolonged depletion of profilin 1 or F-actin causes an adaptive response in microtubules.The Journal of cell biology · 2024Article
- Tau oligomerization on microtubules in health and disease.Cytoskeleton (Hoboken, N.J.) · 2024Article
- Cytoskeletal adaptation following long-term dysregulation of actomyosin in neuronal processes.bioRxiv : the preprint server for biology · 2023Article
- VASH1-SVBP and VASH2-SVBP generate different detyrosination profiles on microtubules.The Journal of cell biology · 2023Article
- Beyond the GTP-cap: Elucidating the molecular mechanisms of microtubule catastrophe.BioEssays : news and reviews in molecular, cellular and developmental biology · 2023Article
- Alzheimer's disease: an axonal injury disease?Frontiers in aging neuroscience · 2023Review
- Cellular cartography: Towards an atlas of the neuronal microtubule cytoskeleton.Frontiers in cell and developmental biology · 2023Review
- Article
- Tau Protein Interaction Partners and Their Roles in Alzheimer's Disease and Other Tauopathies.International journal of molecular sciences · 2021Review
- Tau, XMAP215/Msps and Eb1 co-operate interdependently to regulate microtubule polymerisation and bundle formation in axons.PLoS genetics · 2021Article
- Epigallocatechin-3-gallate modulates Tau Post-translational modifications and cytoskeletal network.Oncotarget · 2021Article
- Beyond Neuronal Microtubule Stabilization: MAP6 and CRMPS, Two Converging Stories.Frontiers in molecular neuroscience · 2021Article
Corrections and comments
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Authors and funding
15 authors at 4 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Proper regulation of microtubule dynamics is essential for cell functions and involves various microtubule-associated proteins (MAPs). Among them, end-binding proteins (EBs) accumulate at microtubule plus ends, whereas structural MAPs bind along the microtubule lattice. Recent data indicate that the structural MAP tau modulates EB subcellular localization in neurons. However, the molecular determinants of EB/tau interaction remain unknown, as is the effect of this interplay on microtubule dynamics. Here we investigate the mechanisms governing EB/tau interaction in cell-free systems and cellular models. We find that tau inhibits EB tracking at microtubule ends. Tau and EBs form a complex via the C-terminal region of EBs and the microtubule-binding sites of tau. These two domains are required for the inhibitory activity of tau on EB localization to microtubule ends. Moreover, the phosphomimetic mutation S262E within tau microtubule-binding sites impairs EB/tau interaction and prevents the inhibitory effect of tau on EB comets. We further show that microtubule dynamic parameters vary, depending on the combined activities of EBs and tau proteins. Overall our results demonstrate that tau directly antagonizes EB function through a phosphorylation-dependent mechanism. This study highlights a novel role for tau in EB regulation, which might be impaired in neurodegenerative disorders.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.